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Database: UniProt
Entry: B7ZC96_DANRE
LinkDB: B7ZC96_DANRE
Original site: B7ZC96_DANRE 
ID   B7ZC96_DANRE            Unreviewed;      1184 AA.
AC   B7ZC96;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   22-NOV-2017, entry version 84.
DE   SubName: Full=Potassium large conductance calcium-activated channel, subfamily M, alpha member 1a {ECO:0000313|Ensembl:ENSDARP00000118939};
GN   Name=kcnma1a {ECO:0000313|Ensembl:ENSDARP00000118939,
GN   ECO:0000313|ZFIN:ZDB-GENE-070202-9};
GN   Synonyms=kcnma1b {ECO:0000313|ZFIN:ZDB-GENE-070202-9};
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Cyprinidae; Danio.
OX   NCBI_TaxID=7955 {ECO:0000313|Ensembl:ENSDARP00000118939, ECO:0000313|Proteomes:UP000000437};
RN   [1] {ECO:0000213|PDB:3U6N}
RP   X-RAY CRYSTALLOGRAPHY (3.61 ANGSTROMS) OF 360-1075 IN COMPLEX WITH
RP   CALCIUM.
RX   PubMed=22139424; DOI=10.1038/nature10670;
RA   Yuan P., Leonetti M.D., Hsiung Y., MacKinnon R.;
RT   "Open structure of the Ca2+ gating ring in the high-conductance Ca2+-
RT   activated K+ channel.";
RL   Nature 481:94-97(2011).
RN   [2] {ECO:0000313|Ensembl:ENSDARP00000118939, ECO:0000313|Proteomes:UP000000437}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000118939,
RC   ECO:0000313|Proteomes:UP000000437};
RX   PubMed=23594743; DOI=10.1038/nature12111;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C.,
RA   Muffato M., Collins J.E., Humphray S., McLaren K., Matthews L.,
RA   McLaren S., Sealy I., Caccamo M., Churcher C., Scott C., Barrett J.C.,
RA   Koch R., Rauch G.J., White S., Chow W., Kilian B., Quintais L.T.,
RA   Guerra-Assuncao J.A., Zhou Y., Gu Y., Yen J., Vogel J.H., Eyre T.,
RA   Redmond S., Banerjee R., Chi J., Fu B., Langley E., Maguire S.F.,
RA   Laird G.K., Lloyd D., Kenyon E., Donaldson S., Sehra H.,
RA   Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA   Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA   Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J.,
RA   Clark S., Pelan S., Griffiths G., Smith M., Glithero R., Howden P.,
RA   Barker N., Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G.,
RA   Lovell J., Beasley H., Henderson C., Gordon D., Auger K., Wright D.,
RA   Collins J., Raisen C., Dyer L., Leung K., Robertson L., Ambridge K.,
RA   Leongamornlert D., McGuire S., Gilderthorp R., Griffiths C.,
RA   Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M., Brown J.,
RA   Murnane C., Gray E., Humphries M., Sycamore N., Barker D.,
RA   Saunders D., Wallis J., Babbage A., Hammond S.,
RA   Mashreghi-Mohammadi M., Barr L., Martin S., Wray P., Ellington A.,
RA   Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA   Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA   Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D.,
RA   Bird C., Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z.,
RA   Eser C., Geiger H., Geisler M., Karotki L., Kirn A., Konantz J.,
RA   Konantz M., Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C.,
RA   Raddatz G., Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C.,
RA   Yang F., Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J.,
RA   Searle S.M., Enright A., Geisler R., Plasterk R.H., Lee C.,
RA   Westerfield M., de Jong P.J., Zon L.I., Postlethwait J.H.,
RA   Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., Rogers J.,
RA   Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the
RT   human genome.";
RL   Nature 496:498-503(2013).
RN   [3] {ECO:0000313|Ensembl:ENSDARP00000118939}
RP   IDENTIFICATION.
RC   STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000118939};
RG   Ensembl;
RL   Submitted (AUG-2013) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the potassium channel family.
CC       {ECO:0000256|SAAS:SAAS00692852}.
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data. {ECO:0000313|Ensembl:ENSDARP00000118939}.
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DR   EMBL; AL645926; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL954192; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BX469897; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CT025847; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; NP_001139072.1; NM_001145600.1.
DR   UniGene; Dr.74676; -.
DR   PDB; 3U6N; X-ray; 3.61 A; A/B/C/D/E/F/G/H=360-1075.
DR   PDBsum; 3U6N; -.
DR   ProteinModelPortal; B7ZC96; -.
DR   SMR; B7ZC96; -.
DR   DIP; DIP-59437N; -.
DR   STRING; 7955.ENSDARP00000105964; -.
DR   PaxDb; B7ZC96; -.
DR   Ensembl; ENSDART00000143200; ENSDARP00000118939; ENSDARG00000079840.
DR   GeneID; 568554; -.
DR   CTD; 568554; -.
DR   ZFIN; ZDB-GENE-070202-9; kcnma1a.
DR   eggNOG; KOG1420; Eukaryota.
DR   eggNOG; ENOG410YUX1; LUCA.
DR   GeneTree; ENSGT00530000063026; -.
DR   HOGENOM; HOG000019856; -.
DR   HOVERGEN; HBG052222; -.
DR   Reactome; R-DRE-1296052; Ca2+ activated K+ channels.
DR   Proteomes; UP000000437; Chromosome 13.
DR   Bgee; ENSDARG00000079840; -.
DR   ExpressionAtlas; B7ZC96; baseline.
DR   GO; GO:0008076; C:voltage-gated potassium channel complex; IEA:InterPro.
DR   GO; GO:0060072; F:large conductance calcium-activated potassium channel activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005249; F:voltage-gated potassium channel activity; IEA:InterPro.
DR   GO; GO:0010996; P:response to auditory stimulus; IMP:ZFIN.
DR   InterPro; IPR024939; Ca-act_K_channel_Slo-1.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR003929; K_chnl_BK_asu.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR028325; VG_K_chnl.
DR   PANTHER; PTHR10027:SF28; PTHR10027:SF28; 1.
DR   Pfam; PF03493; BK_channel_a; 1.
DR   Pfam; PF00520; Ion_trans; 1.
DR   PRINTS; PR00169; KCHANNEL.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   1: Evidence at protein level;
KW   3D-structure {ECO:0000213|PDB:3U6N}; Calcium {ECO:0000213|PDB:3U6N};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000437};
KW   Ion channel {ECO:0000256|SAAS:SAAS00417203};
KW   Ion transport {ECO:0000256|SAAS:SAAS00417186};
KW   Membrane {ECO:0000256|SAAS:SAAS00788393, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000213|PDB:3U6N};
KW   Potassium {ECO:0000256|SAAS:SAAS00417282};
KW   Potassium channel {ECO:0000256|SAAS:SAAS00417246};
KW   Potassium transport {ECO:0000256|SAAS:SAAS00417240};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000437};
KW   Transmembrane {ECO:0000256|SAAS:SAAS00793138,
KW   ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAAS:SAAS00789957,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|SAAS:SAAS00417268}.
FT   TRANSMEM     39     61       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    133    151       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    171    189       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    254    275       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    291    309       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    321    339       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN      134    345       Ion_trans. {ECO:0000259|Pfam:PF00520}.
FT   METAL       468    468       Calcium. {ECO:0000213|PDB:3U6N}.
FT   METAL       908    908       Calcium; via carbonyl oxygen.
FT                                {ECO:0000213|PDB:3U6N}.
FT   METAL       911    911       Calcium; via carbonyl oxygen.
FT                                {ECO:0000213|PDB:3U6N}.
FT   METAL       914    914       Calcium. {ECO:0000213|PDB:3U6N}.
FT   METAL       916    916       Calcium. {ECO:0000213|PDB:3U6N}.
SQ   SEQUENCE   1184 AA;  133326 MW;  70515565BD1DF9E6 CRC64;
     MSNNINFNKN PDSSVSISKM DVIIPFTPDV PCDNNGQRMW WAFLASSMVT FFGGLFIILL
     WRTLKYLWTV CCHCNIKNKE AQKVNNPITI QADGTTKTGN EKEEAPASEV GWMTSVKDWA
     GVMISAQTLT GRVLVVLVFA LSIGALGIYF IDSSDPIESC QNFYKDFTLQ IDMAFNVFFL
     LYFGLRFIAA NDKLWFWLEV NSVVDFFTVP PVFVSVYLNR SWLGLRFLRA LRLIQFSEIL
     QFLNILKTSN SIKLVNLCSI FISTWLTAAG FIHLVENSGD PWENFQNSQP LSYWECVYLL
     MVTMSTVGYG DVYARTTLGR LFMVFFILGG LAMFASYVPE IIELIGNRKK YGGSYSAVNG
     RKHIVVCGHI TLESVSNFLK DFLHKDRDDV NVEIVFLHNI SPNLELEALF KRHFTQVEFY
     QGSVLNPHDL ARVKIESADA CLILANKYCA DPDAEDASNI MRVISIKNYH PKIRIITQML
     QYHNKAHLLN IPSWNWKEGD DAICLAELKA GFIAQSCLAQ GLSTMLANLF SMRSYIKIEE
     DTWQKYYLEG VANEMYTEYL SSAFVGLSFP TVCELCYVKL KLLLIAIEYK SEQRESSILI
     NPGNHVKMQE GTLGFFIASD AKEVKRAFFY CKACHDDITD PKRIKKCGCK RIEDEHPSTL
     SPKKKQRNGG MRNSPNCSPK MMRHDPLLIP GNEQIESMDA NVKRYDSTGM FHWCPSKEIE
     KVILTRSEAS MTVLSGHVVV CIFGDVTSAL VGLRNLVMPL RASNFHYHEL KPIVFVGSLD
     YLRREWETLH NFPKVFILPG TPLSRADLRA VNINLCDMCV ILSANQNNID DASLQDKECI
     LASLNIKSMQ FDDSIGVLQA NSQGFTPPGM DRSSPDNSPV HGLVRQASVT TGSNIPIITE
     LVNDSNVQFL DQDDDDDPDT ELYLTQPFAC GTAFAVSVLD SLMSATYFND NILTLIRTLV
     TGGATPELEA LLAEENALRG GYSTPQTLAN RDRCRVAQLA LYDGPFADLG DGGCYGDLFC
     KALKTYNMLC FGIYRLRDAH LGAPSQCTKR YVITNPPYEF EMVPTDLIFC LMQFDHNAGQ
     SRASLSHSSH SSHSSSKKSS SVHSIPATNR QNRSSKAREA RDKQNATRMN RMGPEKRWFT
     DEAENAYPRN IQIKPMSTHM ANQVNQYKST SSLIPPIREV EDEC
//
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